Amino acid chalcogen analogues as tools in peptide and protein research.
methoxinine
peptides
proteins
redox potentials
selenocysteine and tellurocysteine
selenomethionine and telluromethionine
β-(thienopyrrolyl)- and β-(selenolopyrrolyl)-alanine
β-selenienylalanine and β-tellurienylalanine
β-thienylalanine
Journal
Journal of peptide science : an official publication of the European Peptide Society
ISSN: 1099-1387
Titre abrégé: J Pept Sci
Pays: England
ID NLM: 9506309
Informations de publication
Date de publication:
Feb 2020
Feb 2020
Historique:
received:
05
09
2019
revised:
16
10
2019
accepted:
21
10
2019
pubmed:
20
12
2019
medline:
20
8
2020
entrez:
20
12
2019
Statut:
ppublish
Résumé
The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium element. In the methionine series, only the sulfur-containing methionine is a proteinogenic amino acid, while selenomethionine and telluromethionine are natural amino acids that are incorporated into proteins most probably because of the tolerance of the methionyl-tRNA synthetase; so far, methoxinine the oxygen analogue has not been discovered in natural compounds. Similarly, the chalcogen analogues of tryptophan and phenylalanine in which the benzene ring has been replaced by the largely isosteric thiophene, selenophene, and more recently, even tellurophene are fully synthetic mimics that are incorporated with more or less efficiency into proteins via the related tryptophanyl- and phenylalanyl-tRNA synthetases, respectively. In the serine/cysteine series, also selenocysteine is a proteinogenic amino acid that is inserted into proteins by a special translation mechanism, while the tellurocysteine is again most probably incorporated into proteins by the tolerance of the cysteinyl-tRNA synthetase. For research purposes, all of these natural and synthetic chalcogen amino acids have been extensively applied in peptide and protein research to exploit their different physicochemical properties for modulating structural and functional properties in synthetic peptides and rDNA expressed proteins as discussed in the following review.
Substances chimiques
Amino Acids
0
Chalcogens
0
HSP70 Heat-Shock Proteins
0
HSP90 Heat-Shock Proteins
0
Immunoglobulin M
0
Peptides
0
Proteins
0
Types de publication
Journal Article
Review
Langues
ger
Sous-ensembles de citation
IM
Pagination
e3232Informations de copyright
© 2019 The Authors. Journal of Peptide Science published by European Peptide Society and John Wiley & Sons Ltd.
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